T. Hintermann et D. Seebach, THE BIOLOGICAL STABILITY OF BETA-PEPTIDES - NO INTERACTIONS BETWEEN ALPHA-PEPTIDIC AND BETA-PEPTIDIC STRUCTURES, Chimia, 51(5), 1997, pp. 244-247
The use of peptides in pharmaceutical applications is always hindered
by the rapid degradation of the peptides by enzymes. Recent work on be
ta-peptides, peptides constructed entirely from beta-amino acids, has
shown that even the short-chain oligomers (6 or 7 residues) exhibit re
markably stable secondary structures. However, before certain applicat
ions of beta-peptides can be considered, an information about their po
ssible interactions or reactions with enzymes must be acquired. Ames t
ests (all negative) have now been performed on a selection of beta-ami
no acids, which would be the result of the enzymatic degradation of a
beta-peptide. Furthermore, digestion experiments using a variety of pe
ptidases and beta-peptides have now shown that beta-peptides, in sharp
contrast to their alpha-peptide counterparts, undergo no degradation.